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Porcine follitropin. The amino-acid sequence of the beta subunit.

Authors :
Closset J
Maghuin-Rogister G
Hennen G
Strosberg AD
Source :
European journal of biochemistry [Eur J Biochem] 1978 May; Vol. 86 (1), pp. 115-20.
Publication Year :
1978

Abstract

The amino acid sequence of the porcine beta subunit has been established by studies of peptides isolated after tryptic, thermolytic and staphylococcal protease treatments of the reduced and carboxymethylated chain. The primary structure of the amino-terminal region of the molecule has been solved by automatic sequencing of the reduced and tritium-labeled carboxymethylated subunit. The amino acid sequence of porcine follitropin beta subunit differs from that of its human counterpart by several amino acid replacements, deletion or addition of one or several residues. The porcine chain appears shorter at both its amino and carboxy-terminal ends. The chemical evolution of follitropin is briefly considered and compared to these of thyrotropin and lutropin.

Details

Language :
English
ISSN :
0014-2956
Volume :
86
Issue :
1
Database :
MEDLINE
Journal :
European journal of biochemistry
Publication Type :
Academic Journal
Accession number :
658036
Full Text :
https://doi.org/10.1111/j.1432-1033.1978.tb12290.x